Uteroglobin/SCGB1A1 蛋白, Human

Uteroglobin/SCGB1A1 Protein displays diverse binding, including phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB), and weakly binds progesterone. It acts as a robust inhibitor of phospholipase A2, structurally forming a disulfide-linked antiparallel homodimer. Controversy surrounds its interaction with LMBR1L, necessitating further investigation. Uteroglobin/SCGB1A1 Protein, Human is the recombinant human-derived Uteroglobin/SCGB1A1 protein, expressed by E. coli , with tag free. The total length of Uteroglobin/SCGB1A1 Protein, Human is 70 a.a., with molecular weight of ~7.9 kDa.

子宫珠蛋白/SCGB1A1 蛋白表现出多种结合能力，包括结合磷脂酰胆碱、磷脂酰肌醇、多氯联苯 (PCB) 的能力，以及弱结合黄体酮的能力。此外，它还是磷脂酶 A2 的有效抑制剂。在结构上，该蛋白质形成二硫键连接的反向平行同二聚体。虽然围绕其与 LMBR1L 的相互作用存在一些争议，但需要进一步研究来澄清这一方面。

Measured by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells. The ED₅₀ for this effect is typically 0.2278 μg/mL, corresponding to a specific activity is 4.390×10³ units/mg.

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  Measured by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells. The ED₅₀ for this effect is typically 0.2278 μg/mL, corresponding to a specific activity is 4.390×10³ units/mg.

Human

E. coli

Tag Free

P11684 (E22-N91)

7356  [NCBI]

EICPSFQRVIETLLMDTPSSYEAAMELFSPDQDMREAGAQLKKLVDTLPQKPRESIIKLMEKIAQSSLCN

Approximately 7.9 kDa

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  Greater than 95% as determined by reducing SDS-PAGE.

无菌粉末.

Lyophilized from a 0.2 μm concentrated solution in PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in sterile distilled water. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US;may vary elsewhere.